ArticleJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology1988
pH-temperature interactions on protein function and hibernation: GDP binding to brown adipose tissue mitochondria.
Article in Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 33 citations in OpenAlex.
- Pediatric Hypothermia: An Ambiguous Issue.International journal of environmental research and public health · 2021Review
- Shifts in metabolic fuel use coincide with maximal rates of ventilation and body surface rewarming in an arousing hibernator.American journal of physiology. Regulatory, integrative and comparative physiology · 2019Article
- Spontaneous daily torpor and fasting-induced torpor in Djungarian hamsters are characterized by distinct patterns of metabolic rate.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2015Article
- Repeated functional convergent effects of NaV1.7 on acid insensitivity in hibernating mammals.Proceedings. Biological sciences · 2014Article
- State-dependent regulation of cortical blood flow and respiration in hamsters: response to hypercapnia during arousal from hibernation.The Journal of physiology · 2003Article
- Inner mitochondrial membrane anion channel is present in brown adipocytes but is not identical with the uncoupling protein.The Journal of membrane biology · 1991Article
- Time-course of blood acid-base state during arousal from hibernation in the European hamster.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 1988Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. [3H]GDP binding to the uncoupling protein of brown adipose tissue was determined on mitochondria isolated from hibernating European hamsters, at two temperatures, 35 and 15 degrees C, and four values of 25pH (pH corrected to 25 degrees C): 6.4, 6.8, 7.2 and 7.6, encompassing the physiological range of pH. Buffer composition was adjusted to get the same pH-temperature relationship as for mammalian blood, in which this relationship is mainly determined by protein imidazole buffers. 2. The maximal binding capacity was independent both of temperature and pH. The dissociation constant KD was highly pH-dependent, but was independent of temperature when 25pH was held constant. Under these conditions, the uncoupling protein thus fully conserves its regulatory properties over the temperature range studied (eurythermal adaptation). 3. The temperature coefficient of the apparent pK' for the pH effect (-0.012 +/- 0.004) differed significantly from that of GDP terminal phosphoryl group, but not from that of blood protein imidazole buffer groups, in good agreement with the imidazole alphastat theory. 4. The results indicate that GDP reaction with the protein involves an electrostatic binding with a titratable group of the protein, probably a sulfhydryl. 5. pH modulation of the uncoupling of brown adipose tissue mitochondria probably permits a reversible control of thermogenesis in the hibernation cycle, heat dissipation being inhibited by respiratory acidosis in deep hibernation, but facilitated by the hyperventilation of arousal.
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